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TitleA Promiscuous De Novo Retro-Aldolase Catalyzes Asymmetric Michael Additions via Schiff Base Intermediates.
Journal, issue, pagesAngew. Chem. Int. Ed. Engl., Vol. 54, Page 5609-5612, Year 2015
Publish dateApr 7, 2014 (structure data deposition date)
AuthorsGarrabou, X. / Beck, T. / Hilvert, D.
External linksAngew. Chem. Int. Ed. Engl. / PubMed:25777153
MethodsX-ray diffraction
Resolution1.2 Å
Structure data

PDB-4pa8:
Crystal structure of a de novo retro-aldolase catalyzing asymmetric Michael additions, with a covalently bound product analog
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

Chemicals

ChemComp-2K6:
(3R)-3-(4-methoxyphenyl)-5-oxohexanenitrile

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • sulfolobus solfataricus (archaea)
KeywordsHYDROLASE / protein engineering / computer-aided design / aldolase / retro-aldolase / Michael addition / enzyme design / directed evolution / substrate specificity / de novo protein / artificial catalyst / enzyme-product analog complex / TIM-barrel fold

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